ID   A0A173X7P1_9BACE        Unreviewed;       859 AA.
AC   A0A173X7P1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   Name=bglX_1 {ECO:0000313|EMBL:CUN47644.1};
GN   ORFNames=ERS852397_00310 {ECO:0000313|EMBL:CUN47644.1};
OS   Bacteroides finegoldii.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=338188 {ECO:0000313|EMBL:CUN47644.1, ECO:0000313|Proteomes:UP000095517};
RN   [1] {ECO:0000313|EMBL:CUN47644.1, ECO:0000313|Proteomes:UP000095517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608840 {ECO:0000313|EMBL:CUN47644.1,
RC   ECO:0000313|Proteomes:UP000095517};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448};
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DR   EMBL; CYZH01000001; CUN47644.1; -; Genomic_DNA.
DR   RefSeq; WP_055278292.1; NZ_JAKNGP010000079.1.
DR   AlphaFoldDB; A0A173X7P1; -.
DR   STRING; 338188.ERS852397_00310; -.
DR   Proteomes; UP000095517; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL BETA GLUCOSIDASE; 1.
DR   PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:CUN47644.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUN47644.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095517};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..859
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008015266"
FT   DOMAIN          682..751
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   859 AA;  94935 MW;  EC7DEA1B05D5B53D CRC64;
     MKFIIKDILI ICLFCCASSL NAQHAFPYKN PLLPTEERVN DLLNRMTLQE KIAQISHLQS
     WDVFDGQKLN TAKLAKMCGD KGYGFFEGFP LTAAQCRKNF RIIQTYLLEQ TRLGIPGFSV
     AESLHGVVHE GSTIYPQNIA IGSTFNPALA YEMTKHIAGE LNTIGVKQVL APCIDVAREL
     RWGRVEESFS EDPFLCARMA VAEVKGYMDH GISPMAKHYG PHGNPLGGLN LASVECGIRD
     LFDVYLKPFE AILAETDILA VMSSYNAWNR EPNSASKFML TDILRDRFGF RGYVYSDWGV
     IDMLKNFHKT ADNDFEAASQ ALTAGLDVEA SSLCFKSLES KVLAGEFDVR YIDRAVKRVL
     RAKFELGLFE DPYLEKNSYR WPLRSKECIS LSRQIADEST VLLKNEGNLL PLDIKKLRSV
     AVIGPNADCV QFGDYTWSKN KEDGITPLQG ICRLAGKKVK VNYAQGCSIA SLNQSGIEEA
     VRAAQQSDVA LLFVGSSSTA FVRHSNAPST SGEGIDLSGV ELTGAQEELI EAVCATGKPV
     VLILVAGKPF AIPFAKKNVP AILVQWYAGE QAGNSIADIL FGKVNPSGKI SFSFPQSSGH
     LPAFYNHLTT DKGFYKEPGT YELPGRDYVF SSPNPLWAFG HGLSYTTFDL VSAIADKTHY
     QAHDTIAVKV KIANSGEVVG KEVVQLYIRD VVSTVMTPIK QLKAFEKISL NPAETKEITL
     KVPIHELYLT DNIGNRYLEP GTFEIKVGTA SDRITHRIFI EVGREPEKTP VIDSPQIIKV
     TPSGEFITVQ GFVRDAQATP VAYVTVRAIS SGQETQTDEK GFYSINLRTD DSIAFVKARF
     ITQQMEVKGR KNINIRLVK
//